BIOMAT Database Logo BIOMAT Database Logo

An iron sulfur protein in the mitochondrial outer membrane, reducible by NADH and NADPH. 1973

D Bäckström, and I Hoffström, and I Gustafsson, and A Ehrenberg

UI MeSH Term Description Entries
D007501 Iron A metallic element with atomic symbol Fe, atomic number 26, and atomic weight 55.85. It is an essential constituent of HEMOGLOBINS; CYTOCHROMES; and IRON-BINDING PROTEINS. It plays a role in cellular redox reactions and in the transport of OXYGEN. Iron-56,Iron 56
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D008297 Male Males
D008566 Membranes Thin layers of tissue which cover parts of the body, separate adjacent cavities, or connect adjacent structures. Membrane Tissue,Membrane,Membrane Tissues,Tissue, Membrane,Tissues, Membrane
D008667 Metalloproteins Proteins that have one or more tightly bound metal ions forming part of their structure. (Dorland, 28th ed) Metalloprotein
D008930 Mitochondria, Liver Mitochondria in hepatocytes. As in all mitochondria, there are an outer membrane and an inner membrane, together creating two separate mitochondrial compartments: the internal matrix space and a much narrower intermembrane space. In the liver mitochondrion, an estimated 67% of the total mitochondrial proteins is located in the matrix. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p343-4) Liver Mitochondria,Liver Mitochondrion,Mitochondrion, Liver
D008995 Monoamine Oxidase An enzyme that catalyzes the oxidative deamination of naturally occurring monoamines. It is a flavin-containing enzyme that is localized in mitochondrial membranes, whether in nerve terminals, the liver, or other organs. Monoamine oxidase is important in regulating the metabolic degradation of catecholamines and serotonin in neural or target tissues. Hepatic monoamine oxidase has a crucial defensive role in inactivating circulating monoamines or those, such as tyramine, that originate in the gut and are absorbed into the portal circulation. (From Goodman and Gilman's, The Pharmacological Basis of Therapeutics, 8th ed, p415) EC 1.4.3.4. Amine Oxidase (Flavin-Containing),MAO,MAO-A,MAO-B,Monoamine Oxidase A,Monoamine Oxidase B,Type A Monoamine Oxidase,Type B Monoamine Oxidase,Tyramine Oxidase,MAO A,MAO B,Oxidase, Monoamine,Oxidase, Tyramine
D009243 NAD A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed) Coenzyme I,DPN,Diphosphopyridine Nucleotide,Nadide,Nicotinamide-Adenine Dinucleotide,Dihydronicotinamide Adenine Dinucleotide,NADH,Adenine Dinucleotide, Dihydronicotinamide,Dinucleotide, Dihydronicotinamide Adenine,Dinucleotide, Nicotinamide-Adenine,Nicotinamide Adenine Dinucleotide,Nucleotide, Diphosphopyridine
D009249 NADP Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed) Coenzyme II,Nicotinamide-Adenine Dinucleotide Phosphate,Triphosphopyridine Nucleotide,NADPH,Dinucleotide Phosphate, Nicotinamide-Adenine,Nicotinamide Adenine Dinucleotide Phosphate,Nucleotide, Triphosphopyridine,Phosphate, Nicotinamide-Adenine Dinucleotide
D004578 Electron Spin Resonance Spectroscopy A technique applicable to the wide variety of substances which exhibit paramagnetism because of the magnetic moments of unpaired electrons. The spectra are useful for detection and identification, for determination of electron structure, for study of interactions between molecules, and for measurement of nuclear spins and moments. (From McGraw-Hill Encyclopedia of Science and Technology, 7th edition) Electron nuclear double resonance (ENDOR) spectroscopy is a variant of the technique which can give enhanced resolution. Electron spin resonance analysis can now be used in vivo, including imaging applications such as MAGNETIC RESONANCE IMAGING. ENDOR,Electron Nuclear Double Resonance,Electron Paramagnetic Resonance,Paramagnetic Resonance,Electron Spin Resonance,Paramagnetic Resonance, Electron,Resonance, Electron Paramagnetic,Resonance, Electron Spin,Resonance, Paramagnetic

Related Publications

D Bäckström, and I Hoffström, and I Gustafsson, and A Ehrenberg
Characterization of the iron-sulfur protein of the mitochondrial outer membrane partially purified from beef kidney cortex.
May 1978, Biochimica et biophysica acta,
D Bäckström, and I Hoffström, and I Gustafsson, and A Ehrenberg
Purification of three iron-sulfur proteins from the iron-protein fragment of mitochondrial NADH-ubiquinone oxidoreductase.
May 1982, Biochemistry,
D Bäckström, and I Hoffström, and I Gustafsson, and A Ehrenberg
Enzymatic reduction of labile iron by organelles of the rat liver. Superior role of an NADH-dependent activity in the outer mitochondrial membrane.
October 2008, Biochimie,
D Bäckström, and I Hoffström, and I Gustafsson, and A Ehrenberg
MitoNEET is an iron-containing outer mitochondrial membrane protein that regulates oxidative capacity.
March 2007, Proceedings of the National Academy of Sciences of the United States of America,
D Bäckström, and I Hoffström, and I Gustafsson, and A Ehrenberg
Outer mitochondrial membrane protein degradation by the proteasome.
January 2007, Novartis Foundation symposium,
D Bäckström, and I Hoffström, and I Gustafsson, and A Ehrenberg
NADH regulates the gating of VDAC, the mitochondrial outer membrane channel.
January 1994, The Journal of biological chemistry,
D Bäckström, and I Hoffström, and I Gustafsson, and A Ehrenberg
NADH-dependent aryl hydrocarbon hydroxylase in rat liver mitochondrial outer membrane.
July 1976, European journal of biochemistry,
D Bäckström, and I Hoffström, and I Gustafsson, and A Ehrenberg
Protein sorting between mitochondrial outer and inner membranes. Insertion of an outer membrane protein into the inner membrane.
May 1992, Biochimica et biophysica acta,
D Bäckström, and I Hoffström, and I Gustafsson, and A Ehrenberg
Resolution of mitochondrial NADH dehydrogenase and isolation of two iron-sulfur proteins.
February 1982, Biochemistry,
D Bäckström, and I Hoffström, and I Gustafsson, and A Ehrenberg
Resolution of complex I and isolation of NADH dehydrogenase and an iron--sulfur protein.
January 1978, Methods in enzymology,
Copied contents to your clipboard!